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Database: UniProt
Entry: A0A145WM56_9GAMM
LinkDB: A0A145WM56_9GAMM
Original site: A0A145WM56_9GAMM 
ID   A0A145WM56_9GAMM        Unreviewed;       434 AA.
AC   A0A145WM56;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-FEB-2019, entry version 13.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=AMD27_01015 {ECO:0000313|EMBL:AMW77619.1};
OS   Acinetobacter sp. TGL-Y2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW77619.1, ECO:0000313|Proteomes:UP000076238};
RN   [1] {ECO:0000313|EMBL:AMW77619.1, ECO:0000313|Proteomes:UP000076238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TGL-Y2 {ECO:0000313|EMBL:AMW77619.1,
RC   ECO:0000313|Proteomes:UP000076238};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|RuleBase:RU000579};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; CP015110; AMW77619.1; -; Genomic_DNA.
DR   RefSeq; WP_067655146.1; NZ_CP015110.1.
DR   EnsemblBacteria; AMW77619; AMW77619; AMD27_01015.
DR   KEGG; acv:AMD27_01015; -.
DR   KO; K00003; -.
DR   OrthoDB; 1464088at2; -.
DR   BioCyc; GCF_001612555:G1ESE-204-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000076238; Chromosome.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR016204; HDH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU000579};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076238};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000579};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076238};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      354    434       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    204    204       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     104    104       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     189    189       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   434 AA;  46815 MW;  EFE102309D827A0B CRC64;
     MKPVRLAILG LGTVGGGALK LLQENAAEIR RRTDREIKIT HVGTRRPRAD LGLADSVKQS
     ADLMEIVRQP DVDIVVEVMG GIHPAYELIM EAMKHGKHVV TANKALLAEH GTALFKAADE
     YKVQIAYEAA VAGGIPIIKV IREGLAANRI DWLAGIINGT GNFILSEMRE KGRTFEDVLA
     EAQELGYAEA DPTFDVEGID AAHKLTILAS CAFGIPLQFD KVFTEGISKI TAQDVKYAED
     LGFRIKHLGI ARRAATGIEL RVHPTLIPDD QLIANVNGVK NAVLVQANAV GPTLYYGAGA
     GAGPTASAVV ADVVDIVRDI LYTEDGAGTI PQLAFENLSD LPILSREEMT TGYYIRINAE
     DQMGVLADVT TILSRAGISI DAIMQQPRLK DLIPIVIMTD PIVESKMDEA LSQIQALPVI
     HGEIVRIRLE SLDN
//
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